Structure and dynamics of the RNAPII CTDsome with Rtt103
| Autoři | |
|---|---|
| Rok publikování | 2017 |
| Druh | Článek v odborném periodiku |
| Časopis / Zdroj | Proceeding of the National Academy of Sciences of the USA |
| Fakulta / Pracoviště MU | |
| Citace | |
| www | http://www.pnas.org/content/114/42/11133.full |
| Doi | http://dx.doi.org/10.1073/pnas.1712450114 |
| Obor | Biofyzika |
| Klíčová slova | CTDsome; SAXS; NMR; X ray; Rtt103; RNA Polymerase II |
| Přiložené soubory | |
| Popis | RNA polymerase II (RNAPII) not only transcribes protein coding genes and many noncoding RNA, but also coordinates transcription and RNA processing. This coordination is mediated by a long C-terminal domain (CTD) of the largest RNAPII subunit, which serves as a binding platform for many RNA/protein-binding factors involved in transcription regulation. In this work, we used a hybrid approach to visualize the architecture of the full-length CTD in complex with the transcription termination factor Rtt103. Specifically, we first solved the structures of the isolated subcomplexes at high resolution and then arranged them into the overall envelopes determined at low resolution by small-angle X-ray scattering. The reconstructed overall architecture of the Rtt103–CTD complex reveals how Rtt103 decorates the CTD platform. |
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